author_facet Nonhoff, Ute
Ralser, Markus
Welzel, Franziska
Piccini, Ilaria
Balzereit, Daniela
Yaspo, Marie-Laure
Lehrach, Hans
Krobitsch, Sylvia
Nonhoff, Ute
Ralser, Markus
Welzel, Franziska
Piccini, Ilaria
Balzereit, Daniela
Yaspo, Marie-Laure
Lehrach, Hans
Krobitsch, Sylvia
author Nonhoff, Ute
Ralser, Markus
Welzel, Franziska
Piccini, Ilaria
Balzereit, Daniela
Yaspo, Marie-Laure
Lehrach, Hans
Krobitsch, Sylvia
spellingShingle Nonhoff, Ute
Ralser, Markus
Welzel, Franziska
Piccini, Ilaria
Balzereit, Daniela
Yaspo, Marie-Laure
Lehrach, Hans
Krobitsch, Sylvia
Molecular Biology of the Cell
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
Cell Biology
Molecular Biology
author_sort nonhoff, ute
spelling Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e06-12-1120 <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules Molecular Biology of the Cell
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series Molecular Biology of the Cell
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title Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_unstemmed Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_full Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_fullStr Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_full_unstemmed Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_short Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_sort ataxin-2 interacts with the dead/h-box rna helicase ddx6 and interferes with p-bodies and stress granules
topic Cell Biology
Molecular Biology
url http://dx.doi.org/10.1091/mbc.e06-12-1120
publishDate 2007
physical 1385-1396
description <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p>
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author Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia
author_facet Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia, Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia
author_sort nonhoff, ute
container_issue 4
container_start_page 1385
container_title Molecular Biology of the Cell
container_volume 18
description <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p>
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spelling Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e06-12-1120 <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules Molecular Biology of the Cell
spellingShingle Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia, Molecular Biology of the Cell, Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules, Cell Biology, Molecular Biology
title Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_full Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_fullStr Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_full_unstemmed Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_short Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
title_sort ataxin-2 interacts with the dead/h-box rna helicase ddx6 and interferes with p-bodies and stress granules
title_unstemmed Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
topic Cell Biology, Molecular Biology
url http://dx.doi.org/10.1091/mbc.e06-12-1120